poly((1,4)-alpha-glucosyl) glycogenin-2 + n orthophosphate => glycogenin-2 + n D-glucose 1-phosphate [PYGL]

Stable Identifier
Reaction [transition]
Homo sapiens
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The phosphorylated PYGL dimer (a form) of glycogen phosphorylase catalyzes the reaction of orthophosphate and poly((1,4)-alpha-glucosyl) glycogenin-2 to form D-glucose 1-phosphate and glycogenin-2. This reaction occurs on the surfaces of cytosolic glycogen granules. Non-phosphorylated PYGL dimers (b form) are catalytically inactive even in the presence of AMP. In the body, this reaction takes place in the liver where its dependence on hormonally stimulated PYGL phosphorylation (and lack of sensitivity to AMP) allow glucose mobilization in response to a demand for glucose from the rest of the body (Newgard et al. 1989; Rath et al. 2000).

Literature References
PubMed ID Title Journal Year
10949035 Activation of human liver glycogen phosphorylase by alteration of the secondary structure and packing of the catalytic core

Danley, DE, Mansour, MN, Ammirati, M, Pandit, J, Schulte, GK, LeMotte, PK, Wasilko, DJ, Fennell, KF, Rath, VL, Hynes, TR

Mol Cell 2000
2667896 The family of glycogen phosphorylases: structure and function

Hwang, PK, Newgard, CB, Fletterick, RJ

Crit Rev Biochem Mol Biol 1989
Catalyst Activity

glycogen phosphorylase activity of PGYL dimer a form [cytosol]

Orthologous Events
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